PMID: 7544577Sep 1, 1995Paper

Platelet phospholipase D is activated by protein kinase C via an integrin alpha IIb beta 3-independent mechanism

The Biochemical Journal
E A MartinsonP Presek

Abstract

Blood platelets contain phospholipase D (PLD) that is rapidly activated following platelet stimulation. It is currently unclear, however, where PLD fits into the signalling cascade that leads to aggregation and secretion. Therefore we investigated the mechanism of activation of PLD in human platelets, using the formation of the PLD-specific product phosphatidylethanol as a measure of PLD activity. PLD was activated by a number of platelet agonists that also cause the activation of protein kinase C, including thrombin, collagen, the Ca2+ ionophore A23187 and the thromboxane A2-mimetic U46619. Phorbol 12-myristate 13-acetate (PMA), a direct activator of protein kinase C, also increased PLD activity. A selective inhibitor of protein kinase C, Ro-31-8220, totally blocked the stimulation of PLD by thrombin or PMA under conditions in which it also inhibited phosphorylation of pleckstrin, the major protein kinase C substrate in platelets. Ro-31-8220 additionally inhibited A23187-stimulated PLD activity, indicating that Ca2+ activation of PLD also occurs via a protein kinase C-dependent pathway. In the presence of the fibrinogen antagonist peptide RGDS, which inhibits fibrinogen binding to integrin alpha IIb beta 3 and allows little or...Continue Reading

Citations

Nov 18, 2008·Platelets·M VorlandH Holmsen
Sep 15, 2012·Journal of Thrombosis and Haemostasis : JTH·I ThielmannB Nieswandt
Jun 25, 2005·Clinical Chemistry·Oliver DanneMartin Möckel
Nov 9, 2010·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·David Stegner, Bernhard Nieswandt
May 5, 1998·Molecular and Cellular Biology·R M WolthuisJ L Bos
Dec 19, 2000·Biochemical and Biophysical Research Communications·S MartinM C Martínez
Jun 8, 2007·Clinica Chimica Acta; International Journal of Clinical Chemistry·Oliver DanneMartin Möckel

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